TNNI3_RABIT
ID TNNI3_RABIT Reviewed; 211 AA.
AC P02646;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Troponin I, cardiac muscle;
DE AltName: Full=Cardiac troponin I;
GN Name=TNNI3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1008822; DOI=10.1042/bj1590633;
RA Grand R.J.A., Wilkinson J.M., Mole L.E.;
RT "The amino acid sequence of rabbit cardiac troponin I.";
RL Biochem. J. 159:633-641(1976).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=588250; DOI=10.1042/bj1670183;
RA Grand R.J.A., Wilkinson J.M.;
RT "The amino acid sequence of rabbit slow-muscle troponin I.";
RL Biochem. J. 167:183-192(1977).
RN [3]
RP PROTEIN SEQUENCE OF 6-36, ACETYLATION AT ALA-1, AND PHOSPHORYLATION AT
RP SER-22 AND SER-23.
RC TISSUE=Heart;
RX PubMed=2226863; DOI=10.1016/0014-5793(90)81046-q;
RA Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.;
RT "A common motif of two adjacent phosphoserines in bovine, rabbit and human
RT cardiac troponin I.";
RL FEBS Lett. 273:41-45(1990).
RN [4]
RP PHOSPHORYLATION AT SER-22.
RX PubMed=958429; DOI=10.1038/262615a0;
RA Solaro R.J., Moir A.J.G., Perry S.V.;
RT "Phosphorylation of troponin I and the inotropic effect of adrenaline in
RT the perfused rabbit heart.";
RL Nature 262:615-617(1976).
CC -!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin
CC filament regulatory complex which confers calcium-sensitivity to
CC striated muscle actomyosin ATPase activity.
CC -!- SUBUNIT: Interacts with TRIM63 (By similarity). Binds to actin and
CC tropomyosin. Interacts with STK4/MST1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P02646; Q96RG2: PASK; Xeno; NbExp=2; IntAct=EBI-8614386, EBI-1042651;
CC -!- PTM: Phosphorylated at Ser-22 and Ser-23 by PRKD1; phosphorylation
CC reduces myofilament calcium sensitivity. Phosphorylated preferentially
CC at Thr-31. Phosphorylation by STK4/MST1 alters its binding affinity to
CC TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylated at Ser-42
CC and Ser-44 by PRKCE; phosphorylation increases myocardium contractile
CC dysfunction (By similarity). Ser-22 is one of three sites in the region
CC of residues 1-48 that are phosphorylated by phosphorylase kinase.
CC {ECO:0000250, ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:958429}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR PIR; A90296; TPRBIC.
DR AlphaFoldDB; P02646; -.
DR SMR; P02646; -.
DR IntAct; P02646; 1.
DR MINT; P02646; -.
DR iPTMnet; P02646; -.
DR PRIDE; P02646; -.
DR InParanoid; P02646; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR021666; Troponin-I_N.
DR InterPro; IPR038077; Troponin_sf.
DR Pfam; PF00992; Troponin; 1.
DR Pfam; PF11636; Troponin-I_N; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Direct protein sequencing; Metal-binding;
KW Muscle protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..211
FT /note="Troponin I, cardiac muscle"
FT /id="PRO_0000186154"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..79
FT /note="Involved in binding TNC"
FT REGION 129..150
FT /note="Involved in binding TNC and actin"
FT SITE 80
FT /note="Involved in TNI-TNT interactions"
FT SITE 97
FT /note="Involved in TNI-TNT interactions"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2226863"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 22
FT /note="Phosphoserine; by PHK, PKA and PKD/PRKD1"
FT /evidence="ECO:0000305|PubMed:2226863,
FT ECO:0000305|PubMed:958429"
FT MOD_RES 23
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000305|PubMed:2226863"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 31
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 42
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 44
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 51
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 129
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 143
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 151
FT /note="Phosphoserine; by PAK3"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT CONFLICT 17
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21..26
FT /note="RSSANY -> SD (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24123 MW; A15B2683C53B2F1C CRC64;
ADESRDAAGE ARPAPAPVRR RSSANYRAYA TEPHAKSKKK ISASRKLQLK TLMLQIAKQE
LEREAEERRG EKGRALSTRC QPLELAGLGF AELQDLCRQL HARVDKVDEE RYDVEAKVTK
NITEIADLTQ KIFDLRGKFK RPTLRLRVRI SADAMMQALL GTRAKETLDL RAHLKQVKKE
DTEKENREVG DWRKNIDLLS GMEGRKKKFE G
